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calf thymus DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
DNAse I converts 100% of 1 microg of supercoiled plasmid DNA to relaxed form in 1 h at 37°C. A 10fold higher concentration of DNAse I converts 98% of 1 microg of supercoiled DNA to linear form and a 100fold higher concentration of the nuclease completely digests the DNA into small fragments
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
calf thymus DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
chromatin + H2O
?
-
-
-
-
?
circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
crab d(A-T) polymer + H2O
5'-hexanucleotides + ?
-
unique polymer of alterating A and T contains about 3% G and C residues integrated into its structure
enriched in C and G, sugar specificity may be limited to the nucleotide following the point of cleavage
?
d-ApApTp + H2O
pTp + d-ApA
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
DNA + H2O
5'-phosphotrinucleotides + ?
-
no preference for any nucleotide
as the main products
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
wild-type enzyme and mutant D99A perform double scission on duplex DNA in presence of Mg2+ and Ca2+, not mutant D201A
-
?
Fc-oligo-SH + H2O
?
-
degradation of a thiolated ferrocenyloligonucleotide, efficiency of DNase I reaction on the electrode is 48, 72, or 73% when treated with 1 microl of 2, 1, or 0.5 micromol ferrocenyloligonucleotide, respectively. DNase I can cleave the oligonucleotide on the gold surface and does not show a nonspecific surface absorption
-
-
?
NO2-Ph-pdTp-NO2Ph + H2O
p-nitrophenol + NO2-Ph-pdT-3'-phosphate
-
rapidly hydrolyzed at a single bond
-
?
salmon sperm DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
salmon testis DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
superhelical form converted to circular-relaxed and linear forms
?
additional information
?
-
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for native DNA
produces nicks on one strand in preference to scission of both strands, autoretardation causes the continuous formation of products which are poorer substrates than those from which they are derived
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
major function is to inflict nicks during early stages of hydrolytic attack on DNA, participation in repair phenomena
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+
in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
hydrolysis of both double- and single-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
immobilized DNase I is used in a bioreactor
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I-DNA interaction alters protein secondary structure, with a major reduction in alpha helix and an increase in beta sheet and random structures, and reveals a partial B-to-A DNA conformational change. No DNA digestion upon protein-DNA complexation
-
-
?
plasmid DNA + H2O
?
-
-
-
-
?
plasmid DNA + H2O
?
-
depending on metal ions, duplex DNA is hydrolyzed by DNase I in a single or double scission mode
-
-
?
additional information
?
-
-
immunization of healthy rabbits with bovine DNase I produces IgGs with intrinsic DNase and RNase activities
-
-
?
additional information
?
-
-
interaction of DNase I with yeast transfer RNA alters protein secondary structure with major reduction of the alpha-helix, and increases the random coil, beta-anti and turn structures, while tRNA remains in the A-conformation. No digestion of tRNA by DNase I in the protein-tRNA complexes
-
-
?
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double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
major function is to inflict nicks during early stages of hydrolytic attack on DNA, participation in repair phenomena
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+
in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
hydrolysis of both double- and single-stranded DNA
-
?
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additional information
-
metal binding and influence on activity, wild-type and mutant enzymes, overview
Ba2+
-
-
Ba2+
-
can substitute for Ca2+, but less effective
Ca2+
-
-
Ca2+
-
2 Ca2+ bound to the enzyme under crystallization conditions
Ca2+
-
activation at 1 mM
Ca2+
-
addition of Ca2+ stabilizes the enzyme, facilitates second cut in double-stranded DNA
Ca2+
-
activation at 0.1 mM
Ca2+
-
resistance to proteolysis conveyed by Ca2+
Ca2+
-
no lag phase in the reaction obtained, if only Ca2+ is present or both Mg2+ and Ca2+ are present, double strand digestion preferred
Ca2+
-
Ca2+-binding causes a conformational change that maintains a more active structure of the enzyme
Ca2+
-
activation synergistic with Mg2+
Ca2+
-
dependent on, D201 and D99 are involved in binding, conformation, protects wild-type and mutant D99A enzymes against trypsin inactivation, not mutant D201A
Ca2+
-
in the absence of Ca2+, but with Mg2+ the DNase cleaved the substrate DNA in a single nicking mode
Ca2+
-
in the presence of Ca2+, native (0.2 U) and inactivated DNase I of 5fold greater enzyme units applied (1.0 U) hydrolyze the Mg2+-DNA substrate forming some linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission, while 0.2 U of 2-nitro-5-thiosulfobenzoic acid-treated DNase I can only cleave the Mg2+-DNA substrate in a single nicking mode
Ca2+
-
two Ca2+ ions that stabilize surface loops as well as an additional metal ion binding site at the active site
Ca2+
-
4 ion-binding pockets, two of them strongly bind Ca2+ while the other two sites coordinate Mg2+
Co2+
-
-
Co2+
-
reaction performs mainly double strand scissions, Co2+ is a better activator than other divalent metals
Co2+
-
can substitute for Mg2+, but only 10% efficiency
Mg2+
-
-
Mg2+
-
only single strand cleavage occurs during the lag period of the reaction if only Mg2+ is present
Mg2+
-
enzyme about 99.5% inactive if Ca2+ contamination is reduced to a minimum, must bind to the substrate, whereas Ca2+ must bind to the enzyme
Mg2+
-
presence of Mg2+ alone leads to cutting only one of the two strands
Mg2+
-
activation synergistic with Ca2+
Mg2+
-
in the absence of Ca2+, only native DNase I cleaves the Mg2+-DNA substrate in a single nicking mode with the formation of only the relaxed open-circular DNA, while the 2-nitro-5-thiosulfobenzoic acid-treated DNase I fails to cleave the plasmid DNA substrate
Mg2+
-
in the presence of Mg2+ only, the wild-type cleaves the Mg2+-DNA substrate in a single nicking mode with the formation of only the relaxed open-circular DNA
Mg2+
-
4 ion-binding pockets, two of them strongly bind Ca2+ while the other two sites coordinate Mg2+
Mn2+
-
-
Mn2+
-
can substitute for Mg2+
Mn2+
-
reaction performs mainly double strand scissions
Mn2+
-
most active, faster production of linear form of supercoiled DNA
Mn2+
-
in the presence of Mn2+, native and 2-nitro-5-thiosulfobenzoic acid-treated DNase I of two different enzyme units used are all able to hydrolyze the plasmid DNA substrate in a double scission mode
Mn2+
-
in the presence of Mn2+, the wild-type is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
Sr2+
-
-
Sr2+
-
can substitute for Ca2+, but less effective
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2-(2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
-
2-(2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
-
2-(2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
-
2-(3-(trifluoromethyl)phenyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-benzyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-mercaptoethanol
-
inactivation, reversal by the addition of 4 mM CaCl2, no inactivation if CaCl2 is present during the reducing reaction
2-Nitro-5-thiocyanobenzoic acid
2-nitro-5-thiosulfobenzoic acid
-
the presence of Ca2+ or Mg2+ at pH 7.5 results in 80% inactivation without fragmentation of the enzyme. In the absence of metal ions it retains 80% of its activity. It binds DNase I through covalent modification, since dialysis and gel filtration can not reverse the inactivation reaction. After dilution into an acid buffer of pH 4.7, the inactivated enzyme regains about 40% of its initial activity. The inhibitor fails to inactivate other enzymes, suggesting that the inhibition is unique to DNase I
actin
-
inhibition of DNase I activity by increasing concentrations of actin dimer. At equimolar actin subunit to DNase I concentration its DNA degrading is inhibited to only about 50%, whereas full inhibition is obtained when the dimer concentration is that of DNase I, i.e., at double monomer concentration, suggesting that only one monomer of the actin dimer is able to inhibit the DNase I activity, although both appear to be able to bind DNase I. Gelsolin segment 1 bound to the dimer inhibits DNase I more effectively than uncomplexed dimer and has a higher affinity to DNase I than dimer alone
Aflatoxin B2a
-
non-competitive inhibitor
Aflatoxin G2
-
non-competitive inhibitor
Aflatoxin G2a
-
non-competitive inhibitor
Aflatoxin M1
-
non-competitive inhibitor
Bile acids
-
inhibit the enzyme in concert with cholesterol sulfate
calf spleen inhibitor protein II
-
molecular weight: 59000 Da, forms an inhibitory uni-uni molecular complex with DNase I, maximum stability at pH 7
-
calf thymus inhibitor protein
-
molecular weight: 49000 Da, maximum stability at pH 6
-
carbodiimide
-
presence of divalent cations slows the rate of inactivation
Cholesterol sulfate
-
from human gastric fluid, the sulfate group and the hydrophobic side chain of cholesterol sulfate are indispensable for the inhibitory effect, irreversible, dependent on bile acids, a ratio of 342:1 of bile acids to cholesterol sulfate is required for complete inhibition
methanesulfonylchloride
-
inactivation at pH 5.0
oligonucleotides
-
competitive inhibition
Trypsin
-
is less resistant to trypsin than human DNase I, DNase I activity decreases gradually
-
2-Nitro-5-thiocyanobenzoic acid
-
inactivation by cleavage of peptide chain at positions 14, 40, 72 and 135
2-Nitro-5-thiocyanobenzoic acid
-
inhibition at identical rates
Ca2+
-
inhibitory above 1 mM
Ca2+
-
slight inhibition of mutant D201A
EDTA
-
-
EDTA
-
current peaks of the Fc-oligo-SH-immobilized electrode are relatively stable within error before and after treatment of DNase I solution with EDTA or RNaseA solution, suggesting that this electrode can be used for the detection of DNase I activity specifically
EGTA
-
-
EGTA
-
inhibition at 0.01 mM in the presence of 2.5 mM Mg2+
G-actin
-
-
-
G-actin
-
DNase I causes depolymerization of F-actin to form a stable complex of 1 mol DNase I with 1 mol G-actin, this complex inhibits DNase I activity
-
iodoacetate
-
inhibition in the presence of Mn2+ or Ca2+ at pH 7.2
iodoacetate
-
formation of a 3-carboxymethyl histidine per molecule, in the presence of 0.1 M Mn2+ gradual inactivation
N-bromosuccinimide
-
modification of Trp19, Trp155 and Trp 178, Trp155 most cruical for activity
N-bromosuccinimide
-
inactivation by modification at Trp155
NaCl
-
-
NaCl
-
Na-DNA is inhibitory
additional information
-
no inhibition by sulfatides and membrane lipids, galactose ceramide, no inhibition by steroid sulfates such as estrone sulfate, pregnenolone sulfate, dehydroepiandrosterone sulfate, no inhibition by DMSO, Tween 20, sodium cholate, and sodium taurocholate
-
additional information
-
DTNB or Na2SO3 alone do not inactivate DNase I, even in the presence of divalent cations
-
additional information
-
thermal stress substantially perturbs the secondary structure of DNase I. Accordingly, heating of solid DNase I samples to temperatures below or above the apparent denaturation temperatures of the solid protein degrades and hence denatures the protein. For denatured DNase I samples, the residual biological activities after heating to 125°C are 37% and the activities after heating to 210°C are ca. 8%. Thermal denaturation of DNase I in high sensitivity differential scanning calorimetry is not reversible upon cooling of thermally denatured proteins (in contrast to lysozyme). Lyophilised lysozyme better refolds than spray-dried DNase I
-
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0.106
2-(2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
Bos taurus
pH and temperature not specified in the publication
0.134
2-(2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
Bos taurus
pH and temperature not specified in the publication
0.148
2-(2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
Bos taurus
pH and temperature not specified in the publication
0.148
2-(3-(trifluoromethyl)phenyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
Bos taurus
pH and temperature not specified in the publication
0.128
2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
Bos taurus
pH and temperature not specified in the publication
0.156
2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
Bos taurus
pH and temperature not specified in the publication
0.197
2-benzyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
Bos taurus
pH and temperature not specified in the publication
0.195
2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
Bos taurus
pH and temperature not specified in the publication
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Delta1-10
inactive enzyme
Delta1-11
inactive enzyme
Delta251-260
inactive enzyme
Delta255-260
inactive enzyme
Delta256-260
inactive enzyme
Delta257-260
inactive enzyme
Delta258-260
inactive enzyme
Delta259-260
inactive enzyme
E102G/S103P
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I activity similar to wild-type, 4fold increase in thioredoxin-like activity
E102P/S103G
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I activity similar to wild-type, 4fold increase in thioredoxin-like activity
G100K/E102P/S103G/G105W
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I activity about half of wild-type, 4.5fold increase in thioredoxin-like activity
G100K/G105W
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I and thioredoxin-like activity similar to wild-type
G100W/E102/G/S103P/G105K
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I activity similar to wild-type, 6fold increase in thioredoxin-like activity
C101A
-
no thioredoxin-like activity as observed for the wild-type
D201A
-
site-directed mutagenesis, exchange of one of 2 Ca2+-binding site residues, 2-3fold increased Km and decrased Vmax compared to the wild-type enzyme, no double-scission ability, no protection by Ca2+ against trypsin inactivation
D99A
-
site-directed mutagenesis, exchange of one of 2 Ca2+-binding site residues, 2-3fold increased Km and unaltered Vmax compared to the wild-type enzyme
F192C/A217C
-
active, more heat stable compared to wild-type
H44A
-
DNase I activity is similar to that of the wild-type
H44D
-
inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode
N106Q
-
enzyme activity is lower than that of the wild-type, is unstable to heat, trypsin resistance is similar to that of the wild-type
N18Q
-
enzyme activity is lower than that of the wild-type, is unstable to heat, trypsin resistance is similar to that of the wild-type
N18Q/N106Q
-
enzyme activity is lower than those of the single mutants, is unstable to heat, trypsin resistance decreases in a time-dependent manner
S43A
-
in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
S43A/H44D
-
inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode
S43C
-
in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
T14A
-
in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
T14A/H44D
-
inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode
T14A/S43A
-
in the presence of Mn2+, though being less active than the wild-type, can still cleave the plasmid DNA in the double scission mode
T14A/S43A/H44D
-
inactive
T14A/S43C
-
DNase I activity is similar to that of the wild-type
T14C
-
in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
T14C/H44D
-
significant increase in DNase I activity
T14C/S43A
-
DNase I activity is similar to that of the wild-type
T14C/S43A/H44D
-
significant increase in DNase I activity
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Chen, C.Y.; Lu, S.C.; Liao, T.H.
Cloning, sequencing and expression of a cDNA encoding bovine pancreatic deoxyribonuclease I in Escherichia coli: purification and characterization of the recombinant enzyme
Gene
206
181-184
1998
Bos taurus
brenda
Bellard, M.; Dretzen, G.; Giangrande, A.; Ramain, P.
Nuclease digestion of transcriptionally active chromatin
Methods Enzymol.
170
317-346
1989
Bos taurus
brenda
Cobianchi, F.; Wilson, S.H.
Enzymes for modifying and labeling DNA and RNA
Methods Enzymol.
152
94-110
1987
Bos taurus
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Bos taurus
brenda
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Bos taurus
brenda
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Bos taurus
brenda
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Bos taurus
brenda
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Bos taurus
brenda
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Bos taurus
brenda
Catley, B.J.
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Bos taurus
brenda
Junowicz, E.; Spencer, J.H.
Studies on bovine pancreatic deoxyribonuclease A 1. Generel properties and activation with different bivalent metals
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Bos taurus
brenda
Poulos, T.L.; Price, P.A.
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Bos taurus
brenda
Schabort, J.C.; Pitout, M.J.
The relationship between the chemical structure of aflatoxins and their effect on bovine pancreas deoxyribonuclease
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Bos taurus
brenda
Laskowski, Sr., M.
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Bos taurus
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brenda
Iwamori, M.; Suzuki, H.; Kimura, T.; Iwamori, Y.
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Bos taurus
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Bos taurus (P00639), Bos taurus
brenda
Bencina, M.; Bencina, K.; Strancar, A.; Podgornik, A.
Immobilization of deoxyribonuclease via epoxy groups of methacrylate monoliths
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Bos taurus
brenda
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Bos taurus
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brenda
Chen, W.J.; Lo, T.; Lai, Y.S.; Huang, P.T.; Lin, C.C.; Liao, T.H.
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brenda
Sato, S.; Fujita, K.; Kanazawa, M.; Mukumoto, K.; Ohtsuka, K.; Waki, M.; Takenaka, S.
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Martnez Valle, F.; Balada, E.; Ordi-Ros, J.; Vilardell-Tarres, M.
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Bos taurus
brenda
Mannherz, H.G.; Ballweber, E.; Hegyi, G.; Goody, R.S.
Cross-linked long-pitch actin dimer forms stoichiometric complexes with gelsolin segment 1 and/or deoxyribonuclease I that nonproductively interact with myosin subfragment 1
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2008
Bos taurus
brenda
Fujihara, J.; Yasuda, T.; Kunito, T.; Fujii, Y.; Takatsuka, H.; Moritani, T; Takeshita, H.
Two N-linked glycosylation sites (Asn18 and Asn106) are both required for full enzymatic activity, thermal stability, and resistance to proteolysis in mammalian deoxyribonuclease I
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Bos taurus, Homo sapiens (P24855), Homo sapiens, Equus caballus (Q4AEE3), Equus caballus
brenda
Elkordy, A.A.; Forbes, R.T.; Barry, B.W.
Study of protein conformational stability and integrity using calorimetry and FT-Raman spectroscopy correlated with enzymatic activity
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Bos taurus
brenda
DiRienzo, J.M.; Cao, L.; Volgina, A.; Bandelac, G.; Korostoff, J..
Functional and structural characterization of chimeras of a bacterial genotoxin and human type I DNAse
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Bos taurus (P00639), Homo sapiens (P24855), Homo sapiens
brenda
Krasnorutskii, M.A.; Buneva, V.N.; Nevinsky, G.A.
Immunization of rabbits with DNase I produces polyclonal antibodies with DNase and RNase activities
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Bos taurus, Homo sapiens
brenda
N'soukpoe-Kossi, C.N.; Tajmir-Riahi, H.A.
DNase I-tRNA interaction
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Bos taurus
brenda
Chen, W.J.; Liao, T.H.
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Bos taurus, Rattus norvegicus
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Chen, W.J.; Huang, P.T.; Cheng, Y.C.; Liao, T.H.
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Bos taurus
brenda
Heddi, B.; Abi-Ghanem, J.; Lavigne, M.; Hartmann, B.
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Bos taurus
brenda
Gueroult, M.; Picot, D.; Abi-Ghanem, J.; Hartmann, B.; Baaden, M.
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Bos taurus
brenda
Zhou, Z.; Zhu, C.; Ren, J.; Dong, S.
A graphene-based real-time fluorescent assay of deoxyribonuclease I activity and inhibition
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2012
Bos taurus
brenda
Nguyen, U.T.; Burrows, L.L.
DNase I and proteinase K impair Listeria monocytogenes biofilm formation and induce dispersal of pre-existing biofilms
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Bos taurus
brenda
Ts Mavrova, A.; Dimov, S.; Yancheva, D.; Kolarevic, A.; Ilic, B.S.; Kocic, G.; Smelcerovic, A.
Synthesis and DNase I inhibitory properties of some 5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidines
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Bos taurus (P00639), Bos taurus
brenda
Brown, H.L.; Hanman, K.; Reuter, M.; Betts, R.P.; van Vliet, A.H.
Campylobacter jejuni biofilms contain extracellular DNA and are sensitive to DNase I treatment
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Bos taurus (P00639)
brenda
Das, T.; Simone, M.; Ibugo, A.I.; Witting, P.K.; Manefield, M.; Manos, J.
Glutathione enhances antibiotic efficiency and effectiveness of DNase I in disrupting Pseudomonas aeruginosa biofilms while also inhibiting pyocyanin activity, thus facilitating restoration of cell enzymatic activity, confluence and viability
Front. Microbiol.
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2429
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Bos taurus (P00639)
brenda
Alexeeva, L.; Patutina, O.; Senkova, A.; Zenkova, M.; Mironova, N.
Inhibition of invasive properties of murine melanoma by bovine pancreatic DNase I in vitro and in vivo
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Bos taurus (P00639), Bos taurus
brenda